FEBS Letters | |
14‐3‐3 proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform‐specific manner and reduce dephosphorylation of Ser‐543 by endogenous protein phosphatases | |
Huber, Steven C.1  Athwal, Gurdeep S.1  Huber, Joan L.1  Wu, Ke2  Ferl, Robert J.2  Bachmann, Markus1  | |
[1] US Department of Agriculture, Agricultural Research Service, and Departments of Horticulture (MB, JLH, GSA), Crop Science and Botany (SCH), North Carolina State University, Raleigh, NC 27695-7631, USA;Department of Horticultural Sciences, University of Florida, Gainesville, FL 32611-0690, USA | |
关键词: Binding site; 14-3-3 Protein; Inhibitor protein; Isoform specificity; Nitrate reductase; Protein phosphatase; Regulatory phosphorylation site; IP; inhibitor protein; NR; NADH; nitrate reductase; NRk; NR; kinase; NR-PP; NR-protein phosphatase; | |
DOI : 10.1016/S0014-5793(96)01188-X | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Three lines of evidence indicate that the 14-3-3 proteins that inactivate the phosphorylated form of spinach leaf NADH:nitrate reductase (NR) bind to the enzyme at the regulatory phosphorylation site (Ser-543). First, a phosphorylated synthetic peptide based on the regulatory site can prevent and also reverse the inactivation of phospho-NR caused by 14-3-3 proteins. Second, sequence-specific and phosphorylation-dependent binding of the aforementioned synthetic peptide to the 14-3-3 proteins was demonstrated in vitro. Third, 14-3-3 proteins were required for the ATP-dependent phosphorylation of NR (as assessed by activity measurements) in the presence of NR-kinase and leaf protein phosphatases. Lastly, we demonstrate specificity of recombinant Arabidopsis 14-3-3 isoforms in the interaction with phospho-NR: ω > χ > ν ⋙ gf, ψ.
【 授权许可】
Unknown
【 预 览 】
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